S-nitrosylation of mouse galectin-2 prevents oxidative inactivation by hydrogen peroxide
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Abstract
type:text
Galectins are a group of animal lectins characterized by their specificity for β-galactosides. Galectin-2 (Gal-2) is predominantly expressed in the gastrointestinal tract. A proteomic analysis identified Gal-2 as a protein that was S-nitrosylated when mouse gastric mucosal lysates were reacted with S-nitrosoglutathione, a physiologically relevant S-nitrosylating agent. In the present study, recombinant mouse (m)Gal-2 was S-nitrosylated using nitrosocysteine (CysNO), which had no effect on the sugar-binding specificity and dimerization capacity of the protein. On the other hand, mGal-2 oxidation by H2O2 resulted in the loss of sugar-binding ability, while S-nitrosylation prevented H2O2-inducted inactivation, presumably by protecting the Cys residue(s) in the protein. These results suggest that S-nitrosylation by nitric oxides protect Gal-2 from oxidative stress in the gastrointestinal tract.
identifier:JOS-j.bbrc.2015.01.055
identifier:http://www.sciencedirect.com/science/article/pii/S0006291X15000856
Journal
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- Biochemical and Biophysical Research Communications
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Biochemical and Biophysical Research Communications 457 (4), 712-717, 2015
Elsevier
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Keywords
Details 詳細情報について
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- CRID
- 1050001202797068928
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- NII Article ID
- 120005575972
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- NII Book ID
- AA00564395
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- ISSN
- 0006291X
- 10902104
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- Text Lang
- en
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- Article Type
- journal article
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- Data Source
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- IRDB
- CiNii Articles